KARG_DROME
ID KARG_DROME Reviewed; 356 AA.
AC P48610; Q8IQB9; Q8IQC0; Q8T0S2; Q9VST5; Q9VST6;
DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot.
DT 24-MAY-2005, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Arginine kinase;
DE Short=AK;
DE EC=2.7.3.3;
GN Name=Argk; ORFNames=CG32031;
OS Drosophila melanogaster (Fruit fly).
OC Eukaryota; Metazoa; Ecdysozoa; Arthropoda; Hexapoda; Insecta; Pterygota;
OC Neoptera; Endopterygota; Diptera; Brachycera; Muscomorpha; Ephydroidea;
OC Drosophilidae; Drosophila; Sophophora.
OX NCBI_TaxID=7227;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORM D).
RA Hecht L.B., Scott L.M., Collier G.E.;
RL Submitted (MAY-1995) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Berkeley;
RX PubMed=10731132; DOI=10.1126/science.287.5461.2185;
RA Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D.,
RA Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F.,
RA George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N.,
RA Sutton G.G., Wortman J.R., Yandell M.D., Zhang Q., Chen L.X., Brandon R.C.,
RA Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C.,
RA Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A.,
RA An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A.,
RA Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V.,
RA Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J.,
RA Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E.,
RA Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B.,
RA Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I.,
RA Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C.,
RA Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S.,
RA Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M.,
RA Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M.,
RA Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D.,
RA Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F.,
RA Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D.,
RA Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A.,
RA Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C.,
RA McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C.,
RA Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L.,
RA Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R.,
RA Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V.,
RA Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F.,
RA Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J.,
RA Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R.,
RA Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y.,
RA Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T.,
RA Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S.,
RA Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W.,
RA Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M.,
RA Venter J.C.;
RT "The genome sequence of Drosophila melanogaster.";
RL Science 287:2185-2195(2000).
RN [3]
RP GENOME REANNOTATION.
RC STRAIN=Berkeley;
RX PubMed=12537572; DOI=10.1186/gb-2002-3-12-research0083;
RA Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S.,
RA Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E.,
RA Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P.,
RA Bettencourt B.R., Celniker S.E., de Grey A.D.N.J., Drysdale R.A.,
RA Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M.,
RA Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E.;
RT "Annotation of the Drosophila melanogaster euchromatic genome: a systematic
RT review.";
RL Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM A).
RC STRAIN=Berkeley; TISSUE=Head;
RX PubMed=12537569; DOI=10.1186/gb-2002-3-12-research0080;
RA Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A.,
RA Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M.,
RA Celniker S.E.;
RT "A Drosophila full-length cDNA resource.";
RL Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-arginine = ADP + H(+) + N(omega)-phospho-L-arginine;
CC Xref=Rhea:RHEA:22940, ChEBI:CHEBI:15378, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:32682, ChEBI:CHEBI:58477, ChEBI:CHEBI:456216; EC=2.7.3.3;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=D;
CC IsoId=P48610-1; Sequence=Displayed;
CC Name=A;
CC IsoId=P48610-2; Sequence=VSP_013807;
CC Name=B;
CC IsoId=P48610-3; Sequence=VSP_013808;
CC Name=C;
CC IsoId=P48610-4; Sequence=VSP_013809;
CC -!- SIMILARITY: Belongs to the ATP:guanido phosphotransferase family.
CC {ECO:0000255|PROSITE-ProRule:PRU00842, ECO:0000255|PROSITE-
CC ProRule:PRU00843}.
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DR EMBL; U26939; AAA68172.1; -; Genomic_DNA.
DR EMBL; U26940; AAA68173.1; -; mRNA.
DR EMBL; AE014296; AAF50325.2; -; Genomic_DNA.
DR EMBL; AE014296; AAF50326.2; -; Genomic_DNA.
DR EMBL; AE014296; AAN11982.1; -; Genomic_DNA.
DR EMBL; AE014296; AAN11983.1; -; Genomic_DNA.
DR EMBL; AY069099; AAL39244.1; -; mRNA.
DR RefSeq; NP_001097556.2; NM_001104086.2. [P48610-1]
DR RefSeq; NP_001286989.1; NM_001300060.1. [P48610-1]
DR RefSeq; NP_523988.2; NM_079264.3. [P48610-1]
DR RefSeq; NP_729446.1; NM_168311.3. [P48610-2]
DR RefSeq; NP_729447.1; NM_168312.3. [P48610-3]
DR RefSeq; NP_729448.1; NM_168313.4. [P48610-4]
DR AlphaFoldDB; P48610; -.
DR SMR; P48610; -.
DR BioGRID; 64445; 60.
DR IntAct; P48610; 33.
DR STRING; 7227.FBpp0076270; -.
DR PaxDb; P48610; -.
DR PRIDE; P48610; -.
DR DNASU; 39041; -.
DR EnsemblMetazoa; FBtr0076543; FBpp0076270; FBgn0000116. [P48610-2]
DR EnsemblMetazoa; FBtr0076544; FBpp0076271; FBgn0000116. [P48610-3]
DR EnsemblMetazoa; FBtr0076545; FBpp0076272; FBgn0000116. [P48610-1]
DR EnsemblMetazoa; FBtr0076546; FBpp0076273; FBgn0000116. [P48610-4]
DR EnsemblMetazoa; FBtr0331550; FBpp0303940; FBgn0000116. [P48610-1]
DR EnsemblMetazoa; FBtr0345030; FBpp0311280; FBgn0000116. [P48610-1]
DR GeneID; 39041; -.
DR KEGG; dme:Dmel_CG32031; -.
DR CTD; 39041; -.
DR FlyBase; FBgn0000116; Argk.
DR VEuPathDB; VectorBase:FBgn0000116; -.
DR eggNOG; KOG3581; Eukaryota.
DR GeneTree; ENSGT00950000182772; -.
DR HOGENOM; CLU_019868_0_0_1; -.
DR InParanoid; P48610; -.
DR PhylomeDB; P48610; -.
DR BRENDA; 2.7.3.3; 1994.
DR SignaLink; P48610; -.
DR BioGRID-ORCS; 39041; 0 hits in 3 CRISPR screens.
DR ChiTaRS; Argk; fly.
DR GenomeRNAi; 39041; -.
DR PRO; PR:P48610; -.
DR Proteomes; UP000000803; Chromosome 3L.
DR Bgee; FBgn0000116; Expressed in second segment of antenna (Drosophila) and 37 other tissues.
DR ExpressionAtlas; P48610; baseline and differential.
DR Genevisible; P48610; DM.
DR GO; GO:0005737; C:cytoplasm; HDA:FlyBase.
DR GO; GO:0005829; C:cytosol; HDA:FlyBase.
DR GO; GO:0005576; C:extracellular region; HDA:FlyBase.
DR GO; GO:0005886; C:plasma membrane; HDA:FlyBase.
DR GO; GO:0004054; F:arginine kinase activity; ISS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004111; F:creatine kinase activity; ISS:FlyBase.
DR GO; GO:0016301; F:kinase activity; IBA:GO_Central.
DR GO; GO:0046314; P:phosphocreatine biosynthetic process; ISS:FlyBase.
DR GO; GO:0016310; P:phosphorylation; ISS:UniProtKB.
DR Gene3D; 1.10.135.10; -; 1.
DR InterPro; IPR000749; ATP-guanido_PTrfase.
DR InterPro; IPR022415; ATP-guanido_PTrfase_AS.
DR InterPro; IPR022414; ATP-guanido_PTrfase_cat.
DR InterPro; IPR022413; ATP-guanido_PTrfase_N.
DR InterPro; IPR036802; ATP-guanido_PTrfase_N_sf.
DR InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR PANTHER; PTHR11547; PTHR11547; 1.
DR Pfam; PF00217; ATP-gua_Ptrans; 1.
DR Pfam; PF02807; ATP-gua_PtransN; 1.
DR SUPFAM; SSF48034; SSF48034; 1.
DR SUPFAM; SSF55931; SSF55931; 1.
DR PROSITE; PS00112; PHOSPHAGEN_KINASE; 1.
DR PROSITE; PS51510; PHOSPHAGEN_KINASE_C; 1.
DR PROSITE; PS51509; PHOSPHAGEN_KINASE_N; 1.
PE 2: Evidence at transcript level;
KW Alternative splicing; ATP-binding; Kinase; Nucleotide-binding;
KW Reference proteome; Transferase.
FT CHAIN 1..356
FT /note="Arginine kinase"
FT /id="PRO_0000211992"
FT DOMAIN 6..91
FT /note="Phosphagen kinase N-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00842"
FT DOMAIN 119..356
FT /note="Phosphagen kinase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 64..68
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 122..126
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 185
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 225
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 229
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 271
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 280..284
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 309..314
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00843"
FT BINDING 314
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1
FT /note="M -> MFALWYLTFAVDEIRKRLAWLFSSNKPAAPALDNKPANPAPAKESAP
FT APAPAPTPKPAVVPPAPKPDPPKPAPAVAKPTPVPVPATAPAPPKEEPAPKPKPEPVPS
FT PVVAPPKPTPPPAKPSSPPKQADKMPIPLPKSLTEANTNGQNGNAANGGNVDELVFGGQ
FT QAEKVLPAAKEASNDFIKGETNAFIQSIKEAQQLGERKQDTM (in isoform A)"
FT /evidence="ECO:0000303|PubMed:12537569"
FT /id="VSP_013807"
FT VAR_SEQ 1
FT /note="M -> MPIPLPKSLTEANTNGQNGNAANGGNVDELVFGGQQAEKVLPAAKEA
FT SNDFIKGETNAFIQSIKEAQQLGERKQDTM (in isoform B)"
FT /evidence="ECO:0000305"
FT /id="VSP_013808"
FT VAR_SEQ 1
FT /note="M -> MGLCASKDKKEKVIEGEVANGEPNGTATAAGAGGDGKQDTM (in
FT isoform C)"
FT /evidence="ECO:0000305"
FT /id="VSP_013809"
FT CONFLICT 1..90
FT /note="Missing (in Ref. 1; AAA68173)"
FT /evidence="ECO:0000305"
FT CONFLICT 42..51
FT /note="VTPTFKSTLL -> GHAHLQVDPA (in Ref. 1; AAA68172)"
FT /evidence="ECO:0000305"
FT CONFLICT 64..66
FT /note="GVG -> ASA (in Ref. 1; AAA68172)"
FT /evidence="ECO:0000305"
FT CONFLICT 85
FT /note="I -> F (in Ref. 1; AAA68172)"
FT /evidence="ECO:0000305"
FT CONFLICT 280
FT /note="R -> L (in Ref. 1; AAA68172)"
FT /evidence="ECO:0000305"
FT CONFLICT 291
FT /note="A -> P (in Ref. 1; AAA68172)"
FT /evidence="ECO:0000305"
FT CONFLICT 309..313
FT /note="RGTRG -> ANPR (in Ref. 1; AAA68172)"
FT /evidence="ECO:0000305"
FT CONFLICT 322
FT /note="V -> S (in Ref. 1; AAA68172)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 356 AA; 39866 MW; 9AD0E80D2CE4F446 CRC64;
MVDAAVLAKL EEGYAKLAAS DSKSLLKKYL TKEVFDNLKN KVTPTFKSTL LDVIQSGLEN
HDSGVGIYAP DAEAYTVFAD LFDPIIEDYH GGFKKTDKHP ASNFGDVSTF GNVDPTNEYV
ISTRVRCGRS MQGYPFNPCL TEAQYKEMES KVSSTLSGLE GELKGKFYPL TGMEKAVQQQ
LIDDHFLFKE GDRFLQAANA CRFWPSGRGI YHNDAKTFLV WCNEEDHLRI ISMQQGGDLG
QIYKRLVTAV NEIEKRVPFS HDDRLGFLTF CPTNLGTTIR ASVHIKVPKL ASNKAKLEEV
AAKYNLQVRG TRGEHTEAEG GVYDISNKRR MGLTEFEAVK EMYDGITELI KLEKSL
